Gershenson A, Gafni A, Steel D
Institute of Gerontology, University of Michigan, Ann Arbor 48109, USA.
Photochem Photobiol. 1998 Apr;67(4):391-8.
Measurement of the room temperature Trp triplet state lifetime in proteins by time-resolved phosphorescence can provide valuable information on the structure and dynamics of proteins in solution. Our time-resolved absorption measurements on the long-lived states resulting from electronic excitation of the chromophore demonstrate the presence of more complex behavior than revealed by time-resolved phosphorescence. To provide additional insight into this behavior, a comparative study of time-resolved transient absorption and time-resolved phosphorescence of proteins in solution was carried out. The results show that the time evolution of the long-lived states observed through transient absorption often differs considerably from that observed in time-resolved phosphorescence. In some proteins, the presence of competing reactions complicates the interpretation of the transient absorption measurements (which may affect the phosphorescence yield). A more complete characterization of these processes will likely prove useful in the study of protein structure and dynamics in solution.
通过时间分辨磷光测量蛋白质中室温色氨酸三重态寿命，可以提供有关溶液中蛋白质结构和动力学的有价值信息。我们对发色团电子激发产生的长寿命态进行的时间分辨吸收测量表明，其行为比时间分辨磷光所揭示的更为复杂。为了进一步深入了解这种行为，我们对溶液中蛋白质的时间分辨瞬态吸收和时间分辨磷光进行了比较研究。结果表明，通过瞬态吸收观察到的长寿命态的时间演化通常与时间分辨磷光中观察到的有很大差异。在某些蛋白质中，竞争反应的存在使瞬态吸收测量的解释变得复杂（这可能会影响磷光产率）。对这些过程进行更全面的表征可能会在溶液中蛋白质结构和动力学的研究中证明是有用的。
